Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Nadia, Perchat"'
Autor:
Nadia Perchat, Christelle Dubois, Rémi Mor-Gautier, Sophie Duquesne, Christophe Lechaplais, David Roche, Stéphanie Fouteau, Ekaterina Darii, Alain Perret
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, 2022, 298 (7), ⟨10.1016/j.jbc.2022.102067⟩
Journal of Biological Chemistry, 2022, 298 (7), ⟨10.1016/j.jbc.2022.102067⟩
International audience; Bacteria adapt to utilize the nutrients available in their environment through a sophisticated metabolic system composed of highly specialized enzymes. Although these en-zymes can metabolize molecules other than those for whic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7c3024256e65c56725547a4a266a3cf
https://hal.inrae.fr/hal-03822699
https://hal.inrae.fr/hal-03822699
Autor:
Valérie A. Delmas, Nadia Perchat, Oriane Monet, Marion Fouré, Ekatarina Darii, David Roche, Ivan Dubois, Emilie Pateau, Alain Perret, Volker Döring, Madeleine Bouzon
Publikováno v:
Metabolic Engineering
Metabolic Engineering, 2022, 72, pp.200-214. ⟨10.1016/j.ymben.2022.03.010⟩
Metabolic Engineering, 2022, 72, pp.200-214. ⟨10.1016/j.ymben.2022.03.010⟩
International audience; The reductive glycine pathway was described as the most energetically favorable synthetic route of aerobic formate assimilation. Here we report the successful implementation of formatotrophy in Escherichia coli by means of a s
Autor:
Alain Perret, Christophe Lechaplais, Sabine Tricot, Nadia Perchat, Carine Vergne, Christine Pellé, Karine Bastard, Annett Kreimeyer, David Vallenet, Anne Zaparucha, Jean Weissenbach, Marcel Salanoubat
Publikováno v:
PLoS ONE, Vol 6, Iss 8, p e22918 (2011)
BackgroundBacteria are key components in all ecosystems. However, our knowledge of bacterial metabolism is based solely on the study of cultivated organisms which represent just a tiny fraction of microbial diversity. To access new enzymatic reaction
Externí odkaz:
https://doaj.org/article/f697af082c04491d853e25a9ad2db1d8
Autor:
Marcel Salanoubat, Christophe Lechaplais, Alain Perret, Nadia Perchat, Ekaterina Darii, Pascal Bazire
Publikováno v:
Journal of Bacteriology
Journal of Bacteriology, 2019, 201 (7), ⟨10.1128/JB.00772-18⟩
Journal of Bacteriology, American Society for Microbiology, 2019, 201 (7), ⟨10.1128/JB.00772-18⟩
Journal of Bacteriology, 2019, 201 (7), ⟨10.1128/JB.00772-18⟩
Journal of Bacteriology, American Society for Microbiology, 2019, 201 (7), ⟨10.1128/JB.00772-18⟩
International audience; L-Carnitine is a trimethylammonium compound mostly known for its contribution to fatty acid transport into mitochondria. In bacteria, it is synthesized from ␥-butyrobetaine (GBB) and can be used as a carbon source. L-Carniti
Autor:
Alexandra Gimbernat, Cécile Fischer, Véronique de Berardinis, Pierre-Loïc Saaidi, Christine Pellé, Jean-Louis Petit, Nadia Perchat, Marielle Besnard-Gonnet, Marcel Salanoubat, Ekaterina Darii, Alain Perret, Maeva Dupont
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, 2018, 115 (19), pp.E4358-E4367. ⟨10.1073/pnas.1722368115⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2018, 115 (19), pp.E4358-E4367. ⟨10.1073/pnas.1722368115⟩
Proceedings of the National Academy of Sciences of the United States of America, 2018, 115 (19), pp.E4358-E4367. ⟨10.1073/pnas.1722368115⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2018, 115 (19), pp.E4358-E4367. ⟨10.1073/pnas.1722368115⟩
International audience; Trigonelline (TG; N-methylnicotinate) is a ubiquitous osmolyte. Although it is known that it can be degraded, the enzymes and metabolites have not been described so far. In this work, we challenged the laboratory model soil-bo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e56f83cb93f0a17a800f5f7dae100b6c
https://hal.science/hal-02323695/document
https://hal.science/hal-02323695/document
Autor:
Alain Perret, Philippe Marlière, Nadia Perchat, Madeleine Bouzon, Valérie Delmas, Frédéric Taran, Jean Weissenbach, Olivier Loreau
Publikováno v:
ACS Synthetic Biology
ACS Synthetic Biology, 2017, 6 (8), pp.1520-1533. ⟨10.1021/acssynbio.7b00029⟩
ACS Synthetic Biology, 2017, 6 (8), pp.1520-1533. ⟨10.1021/acssynbio.7b00029⟩
One-carbon metabolism is an ubiquitous metabolic pathway that encompasses the reactions transferring formyl-, hydroxymethyl- and methyl-groups bound to tetrahydrofolate for the synthesis of purine nucleotides, thymidylate, methionine and dehydropanto
Autor:
Marco Bellinzoni, François Artiguenave, Pedro M. Alzari, Anne Zaparucha, Carine Vergne, Georges N. Cohen, Raquel C. de Melo-Minardi, Nadia Perchat, Alain Perret, Karine Bastard, Jean Weissenbach, Marcel Salanoubat, Tristan Wagner
Publikováno v:
Journal of Biological Chemistry. 286:27399-27405
The exponential increase in genome sequencing output has led to the accumulation of thousands of predicted genes lacking a proper functional annotation. Among this mass of hypothetical proteins, enzymes catalyzing new reactions or using novel ways to
Autor:
Marcel Salanoubat, Alain Perret, Véronique de Berardinis, Aude Papeil, Cécile Fischer, Marielle Besnard, Sabine Tricot, Magalie Michiel, Nadia Perchat
Publikováno v:
Environmental Microbiology Reports.
Summary In aerobic cells, urate is oxidized to 5-hydroxyisourate by two distinct enzymes: a coenzyme-independent urate oxidase (EC 1.7.3.3) found in eukaryotes and bacteria like Bacillus subtilis and a prokaryotic flavoprotein urate hydroxylase (HpxO
Autor:
Magalie, Michiel, Nadia, Perchat, Alain, Perret, Sabine, Tricot, Aude, Papeil, Marielle, Besnard, Véronique, de Berardinis, Marcel, Salanoubat, Cécile, Fischer
Publikováno v:
Environmental microbiology reports. 4(6)
In aerobic cells, urate is oxidized to 5-hydroxyisourate by two distinct enzymes: a coenzyme-independent urate oxidase (EC 1.7.3.3) found in eukaryotes and bacteria like Bacillus subtilis and a prokaryotic flavoprotein urate hydroxylase (HpxO) origin
Autor:
Jean Weissenbach, Marcel Salanoubat, Anne Zaparucha, Nadia Perchat, Christine Pellé, Carine Vergne, Annett Kreimeyer, Sabine Tricot, David Vallenet, Christophe Lechaplais, Karine Bastard, Alain Perret
Publikováno v:
PLoS ONE
PLoS ONE, Vol 6, Iss 8, p e22918 (2011)
PLoS ONE, Vol 6, Iss 8, p e22918 (2011)
BackgroundBacteria are key components in all ecosystems. However, our knowledge of bacterial metabolism is based solely on the study of cultivated organisms which represent just a tiny fraction of microbial diversity. To access new enzymatic reaction